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4d50

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Revision as of 17:20, 9 March 2017

Structure of human deoxyhypusine hydroxylase

Structural highlights

4d50 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4d4z
Activity:	Deoxyhypusine monooxygenase, with EC number 1.14.99.29
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DOHH_HUMAN] Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.[HAMAP-Rule:MF_03101]^[1] ^[2]

Publication Abstract from PubMed

Deoxyhypusine hydroxylase (DOHH) is a non-heme diiron enzyme involved in the posttranslational modification of a critical lysine residue of eukaryotic translation initiation factor 5A (eIF-5A) to yield the unusual amino acid residue hypusine. This modification is essential for the role of eIF-5A in translation and in nuclear export of a group of specific mRNAs. The diiron center of human DOHH (hDOHH) forms a peroxo-diiron(III) intermediate (hDOHHperoxo) when its reduced form reacts with O2. hDOHHperoxo has a lifetime exceeding that of the peroxo intermediates of other diiron enzymes by several orders of magnitude. Here we report the 1.7-A crystal structures of hDOHHperoxo and a complex with glycerol. The structure of hDOHHperoxo reveals the presence of a mu-1,2-peroxo-diiron(III) species at the active site. Augmented by UV/Vis and Mossbauer spectroscopic studies, the crystal structures offer explanations for the extreme longevity of hDOHHperoxo and illustrate how the enzyme specifically recognizes its only substrate, deoxyhypusine-eIF-5A.

Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination.,Han Z, Sakai N, Bottger LH, Klinke S, Hauber J, Trautwein AX, Hilgenfeld R Structure. 2015 Apr 9. pii: S0969-2126(15)00080-5. doi:, 10.1016/j.str.2015.03.002. PMID:25865244^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Park JH, Aravind L, Wolff EC, Kaevel J, Kim YS, Park MH. Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: a HEAT-repeat-containing metalloenzyme. Proc Natl Acad Sci U S A. 2006 Jan 3;103(1):51-6. Epub 2005 Dec 21. PMID:16371467 doi:http://dx.doi.org/0509348102
↑ Vu VV, Emerson JP, Martinho M, Kim YS, Munck E, Park MH, Que L Jr. Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center. Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14814-9. doi:, 10.1073/pnas.0904553106. Epub 2009 Aug 19. PMID:19706422 doi:http://dx.doi.org/10.1073/pnas.0904553106
↑ Han Z, Sakai N, Bottger LH, Klinke S, Hauber J, Trautwein AX, Hilgenfeld R. Crystal Structure of the Peroxo-diiron(III) Intermediate of Deoxyhypusine Hydroxylase, an Oxygenase Involved in Hypusination. Structure. 2015 Apr 9. pii: S0969-2126(15)00080-5. doi:, 10.1016/j.str.2015.03.002. PMID:25865244 doi:http://dx.doi.org/10.1016/j.str.2015.03.002

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d50"

Categories: Deoxyhypusine monooxygenase | Han, Z | Hilgenfeld, R | Sakai, N | Oxidoreductase

@@ Line 1: / Line 1: @@
 ==Structure of human deoxyhypusine hydroxylase==
 <StructureSection load='4d50' size='340' side='right' caption='[[4d50]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d4z|4d4z]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyhypusine_monooxygenase Deoxyhypusine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.29 1.14.99.29] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d50 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d50 RCSB], [http://www.ebi.ac.uk/pdbsum/4d50 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d50 OCA], [http://pdbe.org/4d50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d50 RCSB], [http://www.ebi.ac.uk/pdbsum/4d50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d50 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4d50" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4d50

From Proteopedia

Revision as of 17:20, 9 March 2017

Structure of human deoxyhypusine hydroxylase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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